Biology ~50/50~ (Part 1)

Front 1

Which of the funtional groups characterizes RNA?

(A) A PO2 group, deoxyribose, and thymine
(B) A PO3 group, ribose, and uracil

Back 1

(B) A PO3 group, ribose, and uracil

Reason:
RNA is made up of a phospahte group that contains a phosphate atom and 3 atoms of oxygen. It has a ribose sugar and contains cytosine, guanine, uracil, and adenine. DNA DOES NOT HAVE URACIL. RNA DOES NOT HAVE THYMINE.

Front 2

Which molecule would contain a polar covalent bond?

(A) NaCl
(B) H2O

Back 2

(B) H20

Reason:
Polar covalent bonds are those in which valence electrons are shared between atoms, but unequally. The 2 atoms involved in the bond must be of differing electronegativites in order to form a polar covalent bond.

Front 3

Which compound would NOT be water-soluable?

(A) Potassium chloride
(B) Fatty Acids

Back 3

(B) Fatty Acids

Reason:
Water dissolves polar and ionic compounds, but can't dissolve oils and nonpolar compounds very well.

Front 4

Three terms associated with the travel of water from the roots up through the vascular tissues of plants are:

(A) cohesion, adhesion, and transpiration
(B) cohesion, hybridization, and transpiration

Back 4

(A) cohesion, adhesion, and transpiration

Reason:
Transpiration is where water evaporates from the leaves of the plants.

Cohesion is where the water molecules stick together due to the hydrogen bonds.

Adhesion is when the water molecules stick to the sides of the plant cells, helping to pull themselves up through the plant against the force of gravity.

Front 5

Contains one or more double bonds. What is it?

(A) Unsaturated fatty acids
(B) Lipids

Back 5

(A) Unsaturated fatty acids

Reason:
Unsaturated fatty acids contain at least one carbon-carbon double bond

Front 6

One of the four major classes of biological molecules that are not polymers. What is it?

(A) Lipids
(B) Peptide bonds

Back 6

(A) Lipids

Reason:
Lipids are the only one of four major classes of biological molecules that are not polymers. They are only grouped together because of their hydrophobicity.

Front 7

Linkages between the monomers of proteins. What is it?

(A) Alpha Helix
(B) Peptide Bonds

Back 7

(B) Peptide Bonds

Reason:
The linkages between the amino acids of proteins are peptide bonds. Peptide bonds are covalent bonds.

Front 8

A secondary structure of proteins. What is it?

(A) Alpha Helix
(B) Unsaturated fatty acids

Back 8

(A) Alpha Helix

Reason:
One common secondary structure of proteins is the alpha helix; another is the beta pleated sheet.

The secondary structure of a protein refers to a section of the polypeptide chain that is repeatedly folded or coiled in a regular pattern. They are the result of regular hydrogen bonding between segments of the polypeptide backbone.

Front 9

The storage form of carbohydrates in plants. What is it?

(A) Nucleus
(B) Cellulose

Back 9

(B) Cellulose

Reason:
Cellulose is the polysaccharide that forms the strong cell walls of plant cells. It's a polymer of glucose.

Front 10

The process by which protein conformation is lost or broken down is what?

(A) decondensation
(B) denaturation

Back 10

(B) denaturation

Reason:
Denaturation is the process by which a protein loses its overall structure, or conformation.

Denatured proteins are biologically inactive, and denaturation can occur as a result of extreme conditions of pH, temperature, or salt concentration.

Front 11

Which law states that every energy transfer increases the amount of entropy in the universe?

(A) The second law of thermodynamics
(B) The free energy law

Back 11

(A) The second law of thermodynamics

Front 12

How do catalysts speed up the chemical reactions?

(A) raising the activation energy of the reaction
(B) lowering the activation energy of the reaction

Back 12

(B) lowering the activation energy of the reaction

Reason:
Catalysts speed up chemical reactions by providing an alternate reaction pathway that lowers the activation energy of the reaction. Less energy is required to start the reaction, so it runs more quickly.

Front 13

It describes inhibtion by an enzyme that is capable of either activating or inhibiting a metabolic pathway. What is it?

(A) Allosteric inhibition
(B) Feedback inhibition

Back 13

(A) Allosteric inhibition

Front 14

A reversible inhibitor that looks similar to the normal substrate and competes for the active site of the enzyme. What is it?

(A) Allosteric inhibition
(B) Competitive inhibitor

Back 14

(B) Competitive inhibitor

Front 15

The process by which the binding of the substrate to the enzyme triggers a favorable conformation change, which causes a similar change in all of the proteins' sub units. What is it?

(A) Cooperativity
(B) Noncompetitive inhibitor

Back 15

(A) Cooperativity

Front 16

The process by which a metabolic pathway is shut off by the product it produces. What is it?

(A) Feedback inhibition
(B) Cooperativity

Back 16

(A) Feedback inhibitor

Front 17

It binds to the enzyme at a site other than the active site, causing the enzyme to change shape and be unable to bind to the substrate. What is it?

(A) Competitive inhibitor
(B) Noncompetitive inhibitor

Back 17

(B) Noncompetitive inhibitor

Front 18

A + B -> AB + energy
Which one best characterizes the reaction represented above?

(A) Exergonic reaction
(B) Anabolism

Back 18

(A) Exergonic reaction

Reason:
An exergonic reaction is a spontaneous chemical reaction in which there is a net release of free energy. Energy is given off in the course of the reaction shown.

Front 19

When a water molecule loses an H+ in solution, and another water molecule accepts the proton, what is the water molecule that accepts the proton called?

(A) A hydroxide ion
(B) A hydronium ion

Back 19

(B) A hydronium ion

Reason:
In this situation, the water that donated the H+ would become a hydroxide ion (OH-), whereas the water that accepted the H+ would become a hydronium ion (H3O+)